ID W0DVQ7_9GAMM Unreviewed; 910 AA.
AC W0DVQ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:AHF00961.1};
GN ORFNames=THIAE_03430 {ECO:0000313|EMBL:AHF00961.1};
OS Thiomicrospira aerophila AL3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF00961.1, ECO:0000313|Proteomes:UP000005380};
RN [1] {ECO:0000313|EMBL:AHF00961.1, ECO:0000313|Proteomes:UP000005380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380};
RG DOE Joint Genome Institute;
RA Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007030; AHF00961.1; -; Genomic_DNA.
DR RefSeq; WP_006459269.1; NZ_CP007030.1.
DR AlphaFoldDB; W0DVQ7; -.
DR STRING; 717772.THIAE_03430; -.
DR KEGG; tao:THIAE_03430; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_2_1_6; -.
DR InParanoid; W0DVQ7; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000005380; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02080; P-type_ATPase_cation; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 738..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 778..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 809..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..92
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 99599 MW; 0E2B53D2755241F8 CRC64;
MTESTQAATR KQPDDTPFNW HANKADKALA HFKSSEQGLS SEQAADRLAE FGPNRIETSQ
RSGPWVRLLR QFNNILIYIL IAAAVGTAFL EHWVDTFVIL AVVLINASIG YVQEGKAEQA
LDAIRNMLSP QAVVLRNGQR QTIEADQLVP GDIVLLQAGD KVPADLRLID TRSLRIEEAV
LTGESVPVEK RTEPVATSAS LGDRLSLAYS GTLVSFGRGR GVVIATGEQT EIGRISAMLS
SVETISTPLL RQTAEFGRIL SIIIIFLSAI IFAFGYWVRD YAAAEMFLAA VSLAVSTIPE
GLPAIMTITL AIGVQKMAKR NAIIRRLPAV ETLGAVTTIC SDKTGTLTRN EMTVQALVTA
DHEYQVTGVG YAPQGSIELA GQMLEQDQLE PALAMGLKGA LLCNDSWLVE KEGDWQVNGD
PTEGALLAAA MKVGLDPQTE AGLCPRTDLI PFESDHKFMA TLHHDHEQQG YIFIKGAPEK
ILAMCQQQRT QQGDLPIDVD FWHQAMEKLA ERGQRVLAIA VKRVPASQLE LGFNDVQDGA
ILLNLFGIID PPREEAIKAV AECHQAGIRV KMITGDHAGT AKAIGLQLGI GDGQTAVTGQ
EIEQMDDQTL QEVVSRVDIF ARTSPEHKLR LVAALQAQGH VTAMTGDGVN DAPALKRADV
GISMGRKGTE ASKEASEMVL ADDNFASIAR AVREGRTVYN NIRKSILHML PTNAGQSLTI
IFAILLAHQL PLTPVQVLWV NMVTSVTLAM ALAFEPTEPG VMRRHPRRPD MPLLSGLMLW
RIPFVALLLW AGTFGHFVYM DMQGVIDEYA RTVAINTLVA GQIFYLFNLR YIDQHVFSMD
GLFGSKAMWI AVGTLVVLQL AFTYAPFMNT LFGTTPIATE DWIRILMFGL LVFILVEMEK
WVRRRYFTAA
//
